Cation and sugar selectivity determinants in a novel family of transport proteins
A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insig...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Poolman, Bert [verfasserIn] Knol, Jan [verfasserIn] Van Der Does, Chris [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford BSL: Blackwell Science Ltd ; 1996 |
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| Umfang: |
Online-Ressource |
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| Reproduktion: |
2003 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 19(1996), 5, Seite 0 |
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volume:19 ; year:1996 ; number:5 ; pages:0 |
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| DOI / URN: |
10.1046/j.1365-2958.1996.397949.x |
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| 520 | |a A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. | ||
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10.1046/j.1365-2958.1996.397949.x doi (DE-627)NLEJ241785758 DE-627 ger DE-627 rakwb Poolman, Bert verfasserin aut Cation and sugar selectivity determinants in a novel family of transport proteins Oxford BSL Blackwell Science Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Knol, Jan verfasserin aut Van Der Does, Chris verfasserin aut Henderson, Peter J. F. oth Liang, Wei-Jun oth Leblanc, Gérard oth Pourcher, Thierry oth Mus-Veteau, Isabelle oth In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 19(1996), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:19 year:1996 number:5 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1996.397949.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 19 1996 5 0 |
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10.1046/j.1365-2958.1996.397949.x doi (DE-627)NLEJ241785758 DE-627 ger DE-627 rakwb Poolman, Bert verfasserin aut Cation and sugar selectivity determinants in a novel family of transport proteins Oxford BSL Blackwell Science Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Knol, Jan verfasserin aut Van Der Does, Chris verfasserin aut Henderson, Peter J. F. oth Liang, Wei-Jun oth Leblanc, Gérard oth Pourcher, Thierry oth Mus-Veteau, Isabelle oth In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 19(1996), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:19 year:1996 number:5 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1996.397949.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 19 1996 5 0 |
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10.1046/j.1365-2958.1996.397949.x doi (DE-627)NLEJ241785758 DE-627 ger DE-627 rakwb Poolman, Bert verfasserin aut Cation and sugar selectivity determinants in a novel family of transport proteins Oxford BSL Blackwell Science Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Knol, Jan verfasserin aut Van Der Does, Chris verfasserin aut Henderson, Peter J. F. oth Liang, Wei-Jun oth Leblanc, Gérard oth Pourcher, Thierry oth Mus-Veteau, Isabelle oth In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 19(1996), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:19 year:1996 number:5 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1996.397949.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 19 1996 5 0 |
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10.1046/j.1365-2958.1996.397949.x doi (DE-627)NLEJ241785758 DE-627 ger DE-627 rakwb Poolman, Bert verfasserin aut Cation and sugar selectivity determinants in a novel family of transport proteins Oxford BSL Blackwell Science Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Knol, Jan verfasserin aut Van Der Does, Chris verfasserin aut Henderson, Peter J. F. oth Liang, Wei-Jun oth Leblanc, Gérard oth Pourcher, Thierry oth Mus-Veteau, Isabelle oth In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 19(1996), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:19 year:1996 number:5 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1996.397949.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 19 1996 5 0 |
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10.1046/j.1365-2958.1996.397949.x doi (DE-627)NLEJ241785758 DE-627 ger DE-627 rakwb Poolman, Bert verfasserin aut Cation and sugar selectivity determinants in a novel family of transport proteins Oxford BSL Blackwell Science Ltd 1996 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. 2003 Blackwell Publishing Journal Backfiles 1879-2005 |2003|||||||||| Knol, Jan verfasserin aut Van Der Does, Chris verfasserin aut Henderson, Peter J. F. oth Liang, Wei-Jun oth Leblanc, Gérard oth Pourcher, Thierry oth Mus-Veteau, Isabelle oth In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 19(1996), 5, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:19 year:1996 number:5 pages:0 http://dx.doi.org/10.1046/j.1365-2958.1996.397949.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 19 1996 5 0 |
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Cation and sugar selectivity determinants in a novel family of transport proteins |
| abstract |
A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. |
| abstractGer |
A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. |
| abstract_unstemmed |
A new family of homologous membrane proteins that transport galactosides–pentoses–hexuronides (GPH) is described. By analysing the aligned amino acid sequences of the GPH family, and by exploiting their different specificities for cations and sugars, we have designed mutations that yield novel insights into the nature of ligand binding sites in membrane proteins. Mutants have been isolated/constructed in the melibiose transport proteins of Escherichia coliKlebsiella pneumoniae and Salmonella typhimurium, and the lactose transport protein of Streptococcus thermophilus which facilitate uncoupled transport or have an altered cation and/or substrate specificity. Most of the mutations map in the amino-terminal region, in or near amphipathic α-helices II and IV, or in interhelix-loop 10–11 of the transport proteins. On the basis of the kinetic properties of these mutants, and the primary and secondary structure analyses presented here, we speculate on the cation binding pocket of this family of transporters. The regulation of the transporters through interaction with, or phosphorylation by, components of the phosphoenolpyruvate:sugar phosphotransferase system is also discussed. |
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Cation and sugar selectivity determinants in a novel family of transport proteins |
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Knol, Jan Van Der Does, Chris Henderson, Peter J. F. Liang, Wei-Jun Leblanc, Gérard Pourcher, Thierry Mus-Veteau, Isabelle |
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